ID C1716_DROME Reviewed; 2313 AA.
AC Q9VYD1; Q1RL18; Q961S6; Q9VYD0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Probable histone-lysine N-methyltransferase CG1716;
DE EC=2.1.1.-;
GN Name=Set2; ORFNames=CG1716;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 478-2313.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404; SER-786; SER-788;
RP SER-2130 AND SER-2131, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Probable histone methyltransferase. Histone methylation gives
CC specific tags for epigenetic transcriptional activation or repression
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF48273.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK84931.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48273.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BT025042; ABE73213.1; -; mRNA.
DR EMBL; AY050232; AAK84931.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001162740.1; NM_001169269.2.
DR RefSeq; NP_572888.2; NM_132660.4.
DR AlphaFoldDB; Q9VYD1; -.
DR SMR; Q9VYD1; -.
DR BioGRID; 58681; 4.
DR IntAct; Q9VYD1; 1.
DR STRING; 7227.FBpp0073610; -.
DR iPTMnet; Q9VYD1; -.
DR PaxDb; 7227-FBpp0073610; -.
DR EnsemblMetazoa; FBtr0301559; FBpp0290774; FBgn0030486.
DR GeneID; 32301; -.
DR KEGG; dme:Dmel_CG1716; -.
DR UCSC; CG1716-RA; d. melanogaster.
DR AGR; FB:FBgn0030486; -.
DR CTD; 32301; -.
DR FlyBase; FBgn0030486; Set2.
DR VEuPathDB; VectorBase:FBgn0030486; -.
DR eggNOG; KOG4442; Eukaryota.
DR GeneTree; ENSGT00940000172873; -.
DR HOGENOM; CLU_000516_0_0_1; -.
DR InParanoid; Q9VYD1; -.
DR OrthoDB; 950362at2759; -.
DR PhylomeDB; Q9VYD1; -.
DR BRENDA; 2.1.1.359; 1994.
DR BioGRID-ORCS; 32301; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32301; -.
DR PRO; PR:Q9VYD1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030486; Expressed in egg cell and 24 other cell types or tissues.
DR ExpressionAtlas; Q9VYD1; baseline and differential.
DR Genevisible; Q9VYD1; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046975; F:histone H3K36 methyltransferase activity; IMP:FlyBase.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IMP:FlyBase.
DR GO; GO:0140946; F:histone H3K4 dimethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0141005; P:retrotransposon silencing by heterochromatin formation; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR042294; SETD2_animal.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR46711; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR PANTHER; PTHR46711:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..2313
FT /note="Probable histone-lysine N-methyltransferase CG1716"
FT /id="PRO_0000259523"
FT DOMAIN 1307..1360
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1362..1479
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1486..1502
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 1963..1996
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DNA_BIND 17..29
FT /note="A.T hook 1"
FT DNA_BIND 197..209
FT /note="A.T hook 2"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2177..2218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 490
FT /note="F -> S (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="C -> R (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="M -> L (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="T -> A (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="N -> K (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="K -> R (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 2148
FT /note="E -> A (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 2179
FT /note="T -> S (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 2202
FT /note="S -> N (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
FT CONFLICT 2215
FT /note="T -> S (in Ref. 4; AAK84931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2313 AA; 256791 MW; 811F133520284E2F CRC64;
MEESGPPSNP SPVASRGRGR GRPPKVALSA LGNTPPHINP SLKHADAEAS PTAPEDQDSG
QSECRRSSRK KIIKFDVRDL LNKNRKAHKI QIEARIDSNP STGHSQSGTT AASTSMSTAT
ASAASASSAA TVSRLFSMFE MSHQSLPPPP PPPTALEIFA KPRPTQSLIV AQVTSEPSAV
GGAHPVQTMA GLPPVTPRKR GRPRKSQLAD AAIIPTVIVP SCSDSDTNST STTTSNMSSD
SGELPGFPIQ KPKSKLRVSL KRLKLGGRLE SSDSGNSPSS SSPEVEPPAL QDENAMDERP
KQEQNLSRMV DAEENSDSDS QIIFIEIETE SPKGEEEQEE GRPVEVEPQD LIDIDMELAK
QEPTPDPEED LDEIMVEVLS GPPSLWSADD EAEEEEDATV QRATPPGKEP AADSCSSAPR
RSRRSAPLSG SSRQGKTLEE TFAEIAAESS KQILEAEESQ DQEEQHILID LIEDTLKSDN
IAASLNKDIF EPKVETKATC GEVVPRPEMV TEDVYITEGI AATLEKSAVV TKPTTEMIAE
TKLSDEVVIE PPLKDESDPK QTEVELPESK PAVNIPKSER ILSAEVETTS SPLVPPECCT
LESVSGPVLL ETSLSTEEKS NENVETTPLK TEAAKEDSPP AAPEEEASNS SEEPNFLLED
YESNQEQVAE DEMMKCNNQK GQKQTPLPEM KEPEKPVAET VSKKEKAMEN PARSSPAIVD
KKVRAGEMEK KVVKSTKGTV PEKKMDSKKS CAAVTPAKQK ESGKSAKEAI LKKETEKEKS
SAKLDSSSPN TLDKKGKDTA QWSPQLQTLP KSSTKPPQES APSVISKTTS NQPAPKEEQH
AAKKGLSDNS PPSVLKAKEK AVSGFVECDA MFKAMDLANA QLRLDEKNKK KLKKVPTKVE
APPKVEPPTA VPVPGQKKSL SGKTSLRRNT VYEDSPNLER NSSPSSDSAQ ANTSAGKLKP
SKVKKKINPR RSTICEAAKD LRSSSSSSTP TREVAASSPV STSSDSSSKR NGSKRTTSDL
DGGSKLDQRR YTICEDRQPE TAIPVPLTKR RFSMHPKASA NPLHDTLLQT AGKKRGRKEG
KESLSRQNSL DSSSSASQGA PKKKALKSAE ILSAALLETE SSESTSSGSK MSRWDVQTSP
ELEAANPFGD IAKFIEDGVN LLKRDKVDED QRKEGQDEVK READPEEDEF AQRVANMETP
ATTPTPSPTQ SNPEDSASTT TVLKELETGG GVRRSHRIKQ KPQGPRASQG RGVASVALAP
ISMDEQLAEL ANIEAINEQF LRSEGLNTFQ LLKENFYRCA RQVSQENAEM QCDCFLTGDE
EAQGHLSCGA GCINRMLMIE CGPLCSNGAR CTNKRFQQHQ CWPCRVFRTE KKGCGITAEL
LIPPGEFIME YVGEVIDSEE FERRQHLYSK DRNRHYYFMA LRGEAVIDAT SKGNISRYIN
HSCDPNAETQ KWTVNGELRI GFFSVKPIQP GEEITFDYQY LRYGRDAQRC YCEAANCRGW
IGGEPDSDEG EQLDEESDSD AEMDEEELEA EPEEGQPRKS AKAKAKSKLK AKLPLATGRK
RKEQTKPKDR EYKAGRWLKP SATGSSSSAE KPPKKPKVNK FQAMLEDPDV VEELSLLRRG
GLKNQQDTLR FSRCLVRAKL LKTRLALLRV LTHGELPCRR LFLDYHGLRL LHAWISENGN
DDQLREALLD TLESLPIPNR TMLSDSRVYQ SVQLWSNSLE QQLAVVPQEK QAALHKRMVA
LLQKWQALPE IFRIPKRERI EQMKEHEREA DRQQKHVHAS TALEDQRERE SSNDRFRQDR
FRRDTTSSRI GKPIRMSGNN TICTITTQQK GSNGAPDGMT RNDNRRRSDI GPPSEQRRTL
SKELRRSLFE RKVALDEAER RVCTEDRLEH ELRCEFFGAD INTDPKQLPF YQKTDTNEWF
NSDDVPVPAP PRTELLTKAL LSPDIDVGQG ATDVEYKLPP GVDPLPPAWN WQVTSDGDIY
YYNLRERISQ WEPPSPEQRL QTLLEENTTQ QPLHELQIDP AVLENELIQV DTDYVGSLSA
KSLAQYIEAK VRERRDLRRS KLVSIRLISP RRDEDRLYNQ LESRKYKENK EKIRRRKELY
RRRKIEVLPD AVDEIPVPGK ALPIQPYLFS SDEEETKVAA IEQPAAEEEQ DSLNMAPSTS
HAAMAALGKA VAQPTGLGTV GKRKLPMPPS VTVKKHRQEQ RSKKVKSSQS PLTATSAREA
HEKFRFEISG HVANFLRPYR KESCTLGRIT SDEDYKFLVN RLSYHITTKE MRYCEVSGNP
LSCTESVKHK SYDFINQYMR QKGPVYKKPA END
//
